2012, Número 1
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Rev Invest Clin 2012; 64 (1)
Localización y distribución celular de p22-phox y p47-phox en neutrófilos humanos de pacientes infectados con VIH
Salmen S, Montilla D, London M, Velázquez D, Berrueta L
Idioma: Español
Referencias bibliográficas: 48
Paginas: 40-51
Archivo PDF: 276.33 Kb.
RESUMEN
Introducción. Durante la infección por el virus de inmunodeficiencia
humana (VIH) se ha descrito una disfunción en la
capacidad de los polimorfonucleares (PMN) para producir
superóxido conforme progresa la enfermedad. El complejo
NADPH-oxidasa, fuente principal de superóxido, está constituido
por varias proteínas: citocromo b558 (conformado por
gp91-phox y p22-phox) y el componente citosólico (p47-phox,
p67-phox y p40-phox). La activación de este complejo enzimático
es regulada, en parte, por la localización y redistribución
de sus componentes en compartimientos subcelulares y su ensamblaje
es inducido durante la activación por agonistas. Alteraciones
en la regulación de la producción de superóxido
durante la infección pudieran ser consecuencia de defectos en
la localización y distribución del complejo NADPH-oxidasa.
Material y métodos. Se emplearon técnicas de fraccionamiento
subcelular, inmunofluorescencia y gradientes de densidad
en sacarosa para analizar la localización y migración de
dos de los principales componentes del complejo (p47-phox y
p22-phox) en PMN de pacientes infectados con VIH.
Resultados.
A diferencia de los controles, previo a la estimulación,
la proteína p22-phox se distribuye hacia la periferia cercana a la
membrana plasmática de los neutrófilos de los pacientes infectados
y una proporción de ella sedimenta en las fracciones
de alta densidad en gradientes de sacarosa y en la fracción
citoplasmática insoluble. Mientras que p47-phox mantiene
una distribución difusa en el citoplasma, independientemente
del estímulo. Estos resultados demuestran alteraciones en la
redistribución de componentes del complejo NADPH-oxidasa
en PMN de pacientes infectados por VIH.
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